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Anesthesia or hypothermia: Warning for Alzheimer's patients
March 12, 2009
Notice to health-care professionals: New research published online in the FASEB Journal shows that slight dips in brain temperature causes build-up of abnormal tau protein Everyone knows that its important to keep a cool head, but a new study published online in The FASEB Journal ( http://www.fasebj.org) shows that for Alzheimer's patients, a cool head may make the disease worse. In the research report, scientists show that a protein associated with Alzheimer's (called "tau") builds up in brain cells at an increased rate when temperatures fall, such as when a patient is anesthetized or experiences hypothermia. This finding should be of immediate concern to surgeons, dentists, and any other health care professionals who anesthetize patients with Alzheimer's or patients at an elevated risk for the disease. "We hope that this research will initiate an interest in taking precautions to limit the impact of anesthesia on the disease," said Emmanuel Planel of Columbia University Medical Center and one of the scientists involved in the work. To make this discovery, the scientists used two groups of mice that make the abnormal tau protein that accumulates in Alzheimer's patients. One group was anesthetized, and one group was not. A week after anesthesia, the two groups were compared for the amount of tau protein clumps in their brain cells. The anesthetized group had more of these clumps than the group that was not anesthetized. Furthermore, in mice showing advanced signs of the disease, the build up of tau proteins occurred faster than in those in the early stages. "Every patient wants a surgeon with a cool head," said Gerald Weissmann, M.D., Editor-in-Chief of The FASEB Journal, "but surgeons might not want the same for their patients. People are anesthetized for all kinds of reasons, even dental work, but this study really should make patients and doctors reconsider whether it's really necessary." Federation of American Societies for Experimental Biology

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Emerging Drugs and Targets for Alzheimer's Disease: Volume 1: Beta-Amyloid, Tau Protein and Glucose Metabolism (RSC Drug Discovery)
by Ana Martinez (Editor), David E Thurston (Editor)
Alzheimer's disease is the most prevalent neurodegenerative disorder in the elderly. A recent study from the Bloomberg School of Public Health recently estimated that over 26 million people were living with the disease in 2006 and that the global prevalence of the disease will grow to 106 million by 2050. By that time, 43 per cent of those living with the disease will need high-level care, equivalent to that of a nursing home. However, even if modest advances in preventing or delaying the disease's progression were made, it could have a huge impact on global public health. According to this study, interventions that could delay the onset of the disease by as little as one year would reduce the prevalence of the disease by 12 million fewer cases in 2050. These figures reinforce how...
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Fatal Attractions: Protein Aggregates in Neurodegenerative Disorders (Research and Perspectives in Alzheimer's Disease)
by V.M.-Y. Lee (Editor), J.Q. Trojanowski (Editor), L. Buee (Editor), Y. Christen (Editor)
In this volume are contributions based on a meeting arranged by the WHO and the Fondation IPSEN. The scientists focus on neurodegenerative disorders like Alzheimer's Disease, Chromosome 17-Linked Dementia, Parkinson's Disease and disorders with tauopathies.
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Präparation und Charakterisierung von klonalen, neuralen Zelllinien, welche das EGFP-Tau-Fusions-Protein stabil exprimieren (German Edition)
by Bernd Kaltwaßer (Author)
Bachelorarbeit, die am 03.09.2004 erfolgreich an einer Universität in Deutschland im Fachbereich Biologie / Chemie eingereicht wurde. Einleitung: Das Zytoskelett ist eine der wichtigsten Determinanten der neuronalen Zytoarchitektur. Wechselwirkungen zwischen dem neuronalen Membrankortex und den Filamenten des Zytoskeletts sind wahrscheinlich stark an der Entwicklung und Degeneration von Nervenzellen beteiligt. Die Fusion von Proteinen mit Fluorophoren wie EGFP ist eine geeignete Methode, um die Verteilung dieser Proteine innerhalb der lebenden Zelle zu beobachten. Die Entwicklung von stabil transfizierten PC12-Zellen mit einem EGFP-Tau-Fusionskonstrukt ermöglicht es daher, die Expression und subzelluläre Verteilung von Tau in lebenden Zellen zu studieren. Ziel des Projektes war es...
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Dying Minds
by A. P. Perdian
Dying Minds is an 8,600 word short story.
D—Dementia A—Alzheimer's
*** What if you were diagnosed with Alzheimer's? How would you react? How would it impact your life?
*** What if someone you love was diagnosed with Alzheimer's? How would it impact your life?
This is the tale of a man in the prime of life who receives a diagnosis of early-onset Alzheimer's. The story deals with how he and his daughter respond to the devastating news—and how his life unravels as the disease progresses.
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Veränderungen der mitochondrialen Funktion bei Tauopathien: Die Mutation P301L im Tau-Protein führt auf funktioneller und struktureller Ebene zu ... humanen Neuroblastoma-Zellen (German Edition)
by Kathrin Schulz (Author)
Als Tauopathien wird eine Gruppe von neurodegenerativen Erkrankungen bezeichnet, die als gemeinsames pathologisches Merkmal ein abnorm verändertes Tau-Protein (MAPT) aufweisen. Der genaue Mechanismus, der bei diesen Erkrankungen zur Neurodegeneration führt und mit Demenz, Parkinsonismus und motorischen Störungen einhergehen kann, ist bisher weitgehend ungeklärt. Nur bei FTDP-17 (frontotemporale Demenz mit Parkinsonismus assoziiert mit Chromosom 17) sind Mutationen im Tau-Gen als Auslöser bekannt. Da mitochondriale Dysfunktion bei vielen neurodegenerativen Erkrankungen eine entscheidende Rolle spielt, wurde anhand eines Zellmodells der Einfluss der Tau-Pathologie untersucht. Es zeigte sich, dass die Mutation TauP301L zu einem deutlich verringerten Gehalt und einer drastisch...
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Good Calories, Bad Calories: Fats, Carbs, and the Controversial Science of Diet and Health
by Gary Taubes (Author)
For decades we have been taught that fat is bad for us, carbohydrates better, and that the key to a healthy weight is eating less and exercising more. Yet despite this advice, we have seen unprecedented epidemics of obesity and diabetes. Taubes argues that the problem lies in refined carbohydrates, like white flour, easily digested starches, and sugars, and that the key to good health is the kind of calories we take in, not the number. In this groundbreaking book, award-winning science writer Gary Taubes shows us that almost everything we believe about the nature of a healthy diet is wrong.
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Peptide Folding, Misfolding, and Nonfolding (Wiley Series in Protein and Peptide Science)
by Reinhard Schweitzer-Stenner (Editor), Vladimir Uversky (Editor)
Sheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseasesWith the discovery of intrinsically disordered proteins and peptides (IDPs), researchers realized that proteins do not necessarily adopt a well defined secondary and tertiary structure in order to perform biological functions. In fact, IDPs play biologically relevant roles, acting as inhibitors, scavengers, and even facilitating DNA/RNA-protein interactions. Due to their propensity for self-aggregation and fibril formation, some IDPs are involved in neurodegenerative diseases such as Parkinson's and Alzheimer's.With contributions from leading researchers, this text reviews the most recent studies, encapsulating our understanding of IDPs. The authors explain how the...
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Tackling tau--a hallmark of tangled memories: advances in the understanding of this brain protein and its role in dementia may one day lead to ... An article from: Mind, Mood & Memory
by Gale Reference Team (Author)
This digital document is an article from Mind, Mood & Memory, published by Thomson Gale on March 1, 2007. The length of the article is 842 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser.
Citation Details Title: Tackling tau--a hallmark of tangled memories: advances in the understanding of this brain protein and its role in dementia may one day lead to effective ways to prevent and treat Alzheimer's disease.(medical research)(Medical condition overview) Author: Gale Reference Team Publication: Mind, Mood & Memory (Magazine/Journal) Date: March 1, 2007 Publisher: Thomson Gale Volume: 3 ...
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Structure and Function of Intrinsically Disordered Proteins
by Peter Tompa (Author), Alan Fersht (Author)
The existence and functioning of intrinsically disordered proteins (IDPs) challenge the classical structure-function paradigm that equates function with a well-defined 3D structure. Uncovering the disordered complement of proteomes and understanding their functioning can extend the structure-function paradigm to herald new breakthroughs in drug development. Structure and Function of Intrinsically Disordered Proteins thoroughly covers the history up to the latest developments in this field. After examining the principles of protein structure, the classical paradigm, and the history of structural disorder, the book focuses on physical techniques for the identification and characterization of IDPs. It discusses proteomic and bioinformatic approaches and shows how IDPs behave under...
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Aggregation of Therapeutic Proteins
by Wei Wang (Editor), Christopher J. Roberts (Editor)
This book gives pharmaceutical scientists an up-to-date resource on protein aggregation and its consequences, and available methods to control or slow down the aggregation process. While significant progress has been made in the past decade, the current understanding of protein aggregation and its consequences is still immature. Prevention or even moderate inhibition of protein aggregation has been mostly experimental. The knowledge in this book can greatly help pharmaceutical scientists in the development of therapeutic proteins, and also instigate further scientific investigations in this area. This book fills such a need by providing an overview on the causes, consequences, characterization, and control of the aggregation of therapeutic proteins.
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